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{{short description|Protein family}}
{{short description|Protein family}}
[[File:Cardiac sarcomere structure.png|thumb|266x266px|Cardiac sarcomere structure, featuring troponin C]]
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[[Image:Troponino.svg|thumb|400px|Troponin]]
{{Infobox diagnostic
| name = Troponin C
| image =
| alt =
| caption =
| pronounce =
| purpose =
| test of = [[Troponin]]
| based on =
| synonyms =
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| DiseasesDB = <!--{{DiseasesDB2|numeric_id}}-->
| ICD10 = <!--{{ICD10|Group|Major|minor|LinkGroup|LinkMajor}} or {{ICD10PCS|code|char1/char2/char3/char4}}-->
| ICD9 =
| ICDO =
| MedlinePlus = <!--article_number-->
| eMedicine = <!--article_number-->
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| OPS301 = <!--{{OPS301|code}}-->
| LOINC = <!--{{LOINC|code}}-->
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[[Image:Troponino.svg|thumb|261x261px|Troponin]]
'''Troponin C''' is a protein which is part of the [[troponin]] complex. It contains four calcium-binding [[EF hand]]s, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of [[thin filament]]s, along with [[actin]] and [[tropomyosin]]. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of [[troponin I]] (TnI). The C lobe can bind either Ca<sup>2+</sup> or Mg<sup>2+</sup>. The N lobe, which binds only Ca<sup>2+</sup>, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.
'''Troponin C''' is a protein which is part of the [[troponin]] complex. It contains four calcium-binding [[EF hand]]s, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of [[thin filament]]s, along with [[actin]] and [[tropomyosin]]. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of [[troponin I]] (TnI). The C lobe can bind either Ca<sup>2+</sup> or Mg<sup>2+</sup>. The N lobe, which binds only Ca<sup>2+</sup>, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.


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== Mutations ==
== Mutations ==
Point mutations can occur in troponin C inducing alterations to Ca<sup>2+</sup> and Mg<sup>2+</sup> binding and protein structure,<ref>{{cite journal | vauthors = Kalyva A, Parthenakis FI, Marketou ME, Kontaraki JE, Vardas PE | title = Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies | journal = Journal of Muscle Research and Cell Motility | volume = 35 | issue = 2 | pages = 161–78 | date = April 2014 | pmid = 24744096 | doi = 10.1007/s10974-014-9382-0 | s2cid = 1726747 }}</ref> leading to abnormalities in muscle contraction.<ref>{{cite journal | vauthors = Cheng Y, Regnier M | title = Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility | journal = Archives of Biochemistry and Biophysics | volume = 601 | pages = 11–21 | date = July 2016 | pmid = 26851561 | pmc = 4899195 | doi = 10.1016/j.abb.2016.02.004 | series = Special Issue: Myofilament Modulation of Contraction }}</ref><ref>{{cite journal | vauthors = Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD | title = A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy | journal = The Journal of Biological Chemistry | volume = 284 | issue = 28 | pages = 19090–100 | date = July 2009 | pmid = 19439414 | pmc = 2707221 | doi = 10.1074/jbc.M109.007021 }}</ref> In cardiac muscle, they are related to [[dilated cardiomyopathy]] (DCM) and [[hypertrophic cardiomyopathy]] (HCM).
Point mutations can occur in troponin C inducing alterations to Ca<sup>2+</sup> and Mg<sup>2+</sup> binding and protein structure,<ref>{{cite journal | vauthors = Kalyva A, Parthenakis FI, Marketou ME, Kontaraki JE, Vardas PE | title = Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies | journal = Journal of Muscle Research and Cell Motility | volume = 35 | issue = 2 | pages = 161–78 | date = April 2014 | pmid = 24744096 | doi = 10.1007/s10974-014-9382-0 | s2cid = 1726747 }}</ref> leading to abnormalities in muscle contraction.<ref>{{cite journal | vauthors = Cheng Y, Regnier M | title = Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility | journal = Archives of Biochemistry and Biophysics | volume = 601 | pages = 11–21 | date = July 2016 | pmid = 26851561 | pmc = 4899195 | doi = 10.1016/j.abb.2016.02.004 | series = Special Issue: Myofilament Modulation of Contraction }}</ref><ref>{{cite journal | vauthors = Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD | title = A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy | journal = The Journal of Biological Chemistry | volume = 284 | issue = 28 | pages = 19090–100 | date = July 2009 | pmid = 19439414 | pmc = 2707221 | doi = 10.1074/jbc.M109.007021 | doi-access = free }}</ref> In cardiac muscle, they are related to [[dilated cardiomyopathy]] (DCM) and [[hypertrophic cardiomyopathy]] (HCM).


These known point mutations are:
These known point mutations are:

Latest revision as of 18:37, 31 August 2023

Cardiac sarcomere structure, featuring troponin C
Troponin C
Test ofTroponin
Troponin

Troponin C is a protein which is part of the troponin complex. It contains four calcium-binding EF hands, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of thin filaments, along with actin and tropomyosin. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of troponin I (TnI). The C lobe can bind either Ca2+ or Mg2+. The N lobe, which binds only Ca2+, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.

Isoforms

[edit]
Troponin C, slow skeletal and cardiac muscles
Identifiers
SymbolTNNC1
HGNC11943
OMIM191040
RefSeqNM_003280
UniProtP63316
Other data
LocusChr. 3 p21.1
Search for
StructuresSwiss-model
DomainsInterPro
Troponin C, skeletal muscle
Identifiers
SymbolTNNC2
HGNC11944
OMIM191039
RefSeqNP_003270.1
UniProtP02585
Other data
LocusChr. 20 q13.12
Search for
StructuresSwiss-model
DomainsInterPro

The tissue specific subtypes are:

Mutations

[edit]

Point mutations can occur in troponin C inducing alterations to Ca2+ and Mg2+ binding and protein structure,[1] leading to abnormalities in muscle contraction.[2][3] In cardiac muscle, they are related to dilated cardiomyopathy (DCM) and hypertrophic cardiomyopathy (HCM).

These known point mutations are:

See also

[edit]

References

[edit]
  1. ^ Kalyva A, Parthenakis FI, Marketou ME, Kontaraki JE, Vardas PE (April 2014). "Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies". Journal of Muscle Research and Cell Motility. 35 (2): 161–78. doi:10.1007/s10974-014-9382-0. PMID 24744096. S2CID 1726747.
  2. ^ Cheng Y, Regnier M (July 2016). "Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility". Archives of Biochemistry and Biophysics. Special Issue: Myofilament Modulation of Contraction. 601: 11–21. doi:10.1016/j.abb.2016.02.004. PMC 4899195. PMID 26851561.
  3. ^ Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD (July 2009). "A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy". The Journal of Biological Chemistry. 284 (28): 19090–100. doi:10.1074/jbc.M109.007021. PMC 2707221. PMID 19439414.
[edit]
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